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Recombinant Human Acetylcholinesterase/ACHE Protein, CF

Catalog #: 7574-CE
3 Citations Datasheet / COA / SDS
Catalog # Availability Size / Price Qty
7574-CE-010
R&D Systems Recombinant Proteins and Enzymes
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Product Details
Citations (3)
FAQs
Reviews
Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Human Acetylcholinesterase/ACHE Protein, CF Summary

Product Specifications

Purity
>90%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to cleave Acetylthiocholine. The specific activity is >500 nmol/min/μg, as measured under the described conditions.
Source
Chinese Hamster Ovary cell line, CHO-derived human Acetylcholinesterase/ACHE protein
Glu32-Leu614, with a C-terminal 6-His tag
Accession #
P22303
N-terminal Sequence
Analysis
Glu32
Predicted Molecular Mass
65 kDa
SDS-PAGE
60-75 kDa, reducing conditions

Product Datasheets

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7574-CE

Product Datasheet
COA
SDS

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

7574-CE

Formulation Supplied as a 0.2 μm filtered solution in Tris and NaCl.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

Assay Procedure

Materials
  • Assay Buffer: 0.1 M Sodium Phosphate, 0.05% (w/v) Brij-35, pH 7.5
  • Recombinant Human Acetylcholinesterase/ACHE (rhACHE) (Catalog # 7574-CE)
  • Substrate: Acetylthiocholine (ATC) (Sigma, Catalog # A5626), 20 mM stock in DMSO
  • 5’,5’-Dithiobis(2-nitrobenzoic acid) (DTNB) (Sigma, Catalog # D-8130), 10 mM stock in DMSO
  • 96-well Clear Plate (Costar, Catalog # 92592)
  • Plate Reader (Model: SpectraMax Plus by Molecular Devices) or equivalent
  1. Dilute rhACHE to 0.002 µg/mL in Assay Buffer.
  2. Dilute Substrate to 200 µM in Assay Buffer containing 100 µM DTNB.
  3. Load 50 µL dilute rhACHE to clear plate. Include a control containing Assay Buffer instead of rhACHE.
  4. Start reaction by adding 50 µL Substrate/DNTB mix.
  5. Read plate in kinetic mode for 5 minutes at an absorbance of 405 nm.
  6. Calculate specific activity:

     Specific Activity (nmol/min/µg) =

 Adjusted Vmax* (OD/min) x well volume (L) x 109 nmol/mol
ext. coeff** (M-1cm-1) x path corr.*** (cm) x amount of enzyme (µg)

     *Adjusted for Substrate Blank 
     **Using the extinction coefficient 13260 M-1cm-1 
     ***Using the path correction 0.32 cm
     Note: the output of many spectrophotometers is in mOD Per Well:
  • rhACHE: 0.0001 µg
  • DTNB: 50 µM
  • ATC: 100 µM
Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: Acetylcholinesterase/ACHE

The classical role of ACHE is to terminate cholinergic neurotransmission by hydrolysis of acetylcholine (ACH) (1). ACHE is thought to be involved in the pathology of Alzheimer's disease (AD) by accelerating the assembly of A beta peptides into fibrillar species through forming complexes with A beta via the peripheral anionic site on ACHE. ACHE inhibitors have been used to delay symptoms of AD patients by virtue of their ability to enhance ACH availability, as well as reduce amyloidogenesis and subsequent neurotoxicity (2). Its involvement in the cholinergic anti-inflammatory pathway connects ACHE with a possible marker of low-grade systemic inflammation in obesity, hypertension, coronary heart disease, and AD (3). Alternative splicing produces three isoforms: an amphipathic form that exists as both monomeric and multimeric forms, a soluble monomeric form lacking the cysteine residue near the C-terminus, and a GPI-anchored dimeric form found in the membranes of erythrocytes (1). The recombinant human ACHE (rhACHE) was expressed as the amphipathic form that consists of soluble monomer and multimeric forms.

References
  1. Grisaru, D. et al. (1999) Eur. J. Biochem, 264:672.
  2. Campbell, V. A. and Gowran, A. (2007) Br. J. Pharm. 152:655.
  3. Das, U. N. (2007) Med. Sci. Monit. 13:RA214.
Entrez Gene IDs
43 (Human); 11423 (Mouse); 83817 (Rat)
Alternate Names
acetylcholinesterase (Yt blood group); Acetylcholinesterase; ACHE; apoptosis-related acetylcholinesterase; ARACHE; EC 3.1.1; EC 3.1.1.7; N-ACHE; Yt blood group; YT

Product Specific Notices

Coomassie is a registered trademark of Imperial Chemical Industries Ltd.

Citations for Recombinant Human Acetylcholinesterase/ACHE Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

3 Citations: Showing 1 - 3
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  1. Hydrolysable Tannins Exhibit Acetylcholinesterase Inhibitory and Anti-Glycation Activities In Vitro and Learning and Memory Function Improvements in Scopolamine-Induced Amnesiac Mice
    Authors: LG Chen, SY Lin, YS Lee, CC Wang, WC Hou
    Biomedicines, 2021-08-23;9(8):.
    Species: Human
    Sample Types: Protein
    Applications: Reference Standard
  2. The botanical origin and antioxidant, anti-BACE1 and antiproliferative properties of bee pollen from different regions of South Korea
    Authors: Y Zou, J Hu, W Huang, L Zhu, M Shao, C Dordoe, YJ Ahn, D Wang, Y Zhao, Y Xiong, X Wang
    BMC Complement Med Ther, 2020-07-25;20(1):236.
    Species: Human
    Sample Types:
    Applications: Enzyme Assay
  3. Modulation of neurological pathways by Salvia officinalis and its dependence on manufacturing process and plant parts used
    Authors: C Tober, R Schoop
    BMC Complement Altern Med, 2019-06-13;19(1):128.
    Species: Human
    Sample Types: Reference Standard
    Applications: Bioassay

FAQs

  1. Which isoform of acetylcholinesterase is this protein?

    • The protein we supply is isoform T, which is also known as ACHE-S (synaptic).

View all Proteins and Enzyme FAQs

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